ZNUC_ANAPZ
ID ZNUC_ANAPZ Reviewed; 243 AA.
AC Q2GJA5;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Zinc import ATP-binding protein ZnuC {ECO:0000255|HAMAP-Rule:MF_01725};
DE EC=7.2.2.20 {ECO:0000255|HAMAP-Rule:MF_01725};
GN Name=znuC {ECO:0000255|HAMAP-Rule:MF_01725}; OrderedLocusNames=APH_0983;
OS Anaplasma phagocytophilum (strain HZ).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Anaplasma; phagocytophilum group.
OX NCBI_TaxID=212042;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HZ;
RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT "Comparative genomics of emerging human ehrlichiosis agents.";
RL PLoS Genet. 2:208-222(2006).
CC -!- FUNCTION: Part of the ABC transporter complex ZnuABC involved in zinc
CC import. Responsible for energy coupling to the transport system.
CC {ECO:0000255|HAMAP-Rule:MF_01725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP(in) + H2O(in) + Zn(2+)(out) = ADP(in) + H(+)(in) +
CC phosphate(in) + Zn(2+)(in); Xref=Rhea:RHEA:29795, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29105, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.20;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01725};
CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ZnuC),
CC two transmembrane proteins (ZnuB) and a solute-binding protein (ZnuA).
CC {ECO:0000255|HAMAP-Rule:MF_01725}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01725}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01725}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Zinc importer
CC (TC 3.A.1.15.5) family. {ECO:0000255|HAMAP-Rule:MF_01725}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD44345.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000235; ABD44345.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_044104290.1; NC_007797.1.
DR AlphaFoldDB; Q2GJA5; -.
DR SMR; Q2GJA5; -.
DR STRING; 212042.APH_0983; -.
DR EnsemblBacteria; ABD44345; ABD44345; APH_0983.
DR GeneID; 56368892; -.
DR KEGG; aph:APH_0983; -.
DR eggNOG; COG1121; Bacteria.
DR HOGENOM; CLU_000604_1_11_5; -.
DR OrthoDB; 1721927at2; -.
DR Proteomes; UP000001943; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015633; F:ABC-type zinc transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR017882; ZnuC.
DR PANTHER; PTHR42734:SF9; PTHR42734:SF9; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS51298; ZNUC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..243
FT /note="Zinc import ATP-binding protein ZnuC"
FT /id="PRO_0000281494"
FT DOMAIN 25..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
FT BINDING 57..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01725"
SQ SEQUENCE 243 AA; 27179 MW; 9E4BE25082204935 CRC64;
MYSGQHIKEP VTRVAGLQKS VLPMLVVDSI TLFYGNRKVI DNVSFSIRPG EIITILGPNG
GGKTSLVRVL VGINQDYIGT IHYTKRPIIA YMPQNFKVNS FMPMTVEYLL LSACWGRGIS
LDLRAVIQYV DISKLLTRQI SELSAGEIQL VLLARCMVMK PDLIVLDEPV SCMDVEAKNN
FYRLIGKLVS KYNISIIMTS HDLHCVMACS DRVICINRSI RCEGTPEEIT ESAKFMSVFP
ENV